STRUCTURE AND EVOLUTION OF CYTOCHROME-OXIDASE

被引：23
|
作者：
SARASTE, M
机构：
[1] European Molecular Biology Laboratory, Heidelberg, D-69012
来源：
ANTONIE VAN LEEUWENHOEK INTERNATIONAL JOURNAL OF GENERAL AND MOLECULAR MICROBIOLOGY | 1994年 / 65卷 / 04期
关键词：
CYTOCHROME C OXIDASE; QUINOL OXIDASE; METAL CENTERS; RESPIRATION; DENITRIFICATION; EVOLUTION;
D O I：
10.1007/BF00872214
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
The structural features of cytochrome oxidases are reviewed in light of their evolution. The substrate specificity (quinol vs. cytochrome c) is reflected in the presence of a unique copper centre (Cu-A) in cytochrome c oxidases. In several lines of evolution, quinol oxidases have independently lost this copper. Also, the most primitive cytochrome c oxidases do not contain this copper, and electron entry takes place via c-type haems. These enzymes, exemplified by the rhizobial FixN complex, probably remind the first oxidases. They are related to the denitrification enzyme nitric oxide reductase.
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页码：285 / 287
页数：3
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